ID RFUA_TREPA Reviewed; 343 AA. AC Q56328; DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 118. DE RecName: Full=ABC transporter riboflavin-binding protein RfuA {ECO:0000305}; DE AltName: Full=Membrane lipoprotein TpN38(b) {ECO:0000305}; DE Flags: Precursor; GN Name=rfuA {ECO:0000303|PubMed:23404400}; GN Synonyms=tpn38 {ECO:0000303|PubMed:8598278}; GN OrderedLocusNames=TP_0298; OS Treponema pallidum (strain Nichols). OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae; OC Treponema. OX NCBI_TaxID=243276; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Nichols; RX PubMed=8598278; DOI=10.1111/j.1574-6968.1996.tb07966.x; RA Stamm L.V., Hardham J.M., Frye J.G.; RT "Expression and sequence analysis of a Treponema pallidum gene, Tpn38(b), RT encoding an exported protein with homology to T. pallidum and Borrelia RT burgdorferi proteins."; RL FEMS Microbiol. Lett. 135:57-63(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nichols; RX PubMed=9665876; DOI=10.1126/science.281.5375.375; RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G., RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A., RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D., RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R., RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A., RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O., RA Venter J.C.; RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete."; RL Science 281:375-388(1998). RN [3] {ECO:0007744|PDB:4IIL} RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 21-343 IN COMPLEX WITH RP RIBOFLAVIN, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, PALMITOYLATION AT RP CYS-20, AND DIACYLGLYCEROL AT CYS-20. RX PubMed=23404400; DOI=10.1128/mbio.00615-12; RA Deka R.K., Brautigam C.A., Biddy B.A., Liu W.Z., Norgard M.V.; RT "Evidence for an ABC-type riboflavin transporter system in pathogenic RT spirochetes."; RL MBio 4:E00615-E00615(2013). CC -!- FUNCTION: Probably part of the ABC transporter complex RfuABCD involved CC in riboflavin import. Binds riboflavin. {ECO:0000269|PubMed:23404400}. CC -!- SUBUNIT: Monomer in solution (PubMed:23404400). The complex is probably CC composed of two ATP-binding proteins (RfuB), two transmembrane proteins CC (RfuC and RfuD) and a solute-binding protein (RfuA) (Probable). CC {ECO:0000269|PubMed:23404400, ECO:0000305|PubMed:23404400}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000305|PubMed:23404400}; Lipid-anchor CC {ECO:0000305|PubMed:23404400}; Periplasmic side CC {ECO:0000305|PubMed:23404400}. CC -!- SIMILARITY: Belongs to the BMP lipoprotein family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U12861; AAB02167.1; -; Genomic_DNA. DR EMBL; AE000520; AAC65287.1; -; Genomic_DNA. DR PIR; D71341; D71341. DR RefSeq; WP_010881747.1; NC_021490.2. DR PDB; 4IIL; X-ray; 1.30 A; A=21-343. DR PDBsum; 4IIL; -. DR AlphaFoldDB; Q56328; -. DR SMR; Q56328; -. DR IntAct; Q56328; 9. DR STRING; 243276.TP_0298; -. DR EnsemblBacteria; AAC65287; AAC65287; TP_0298. DR GeneID; 57878835; -. DR KEGG; tpa:TP_0298; -. DR eggNOG; COG1744; Bacteria. DR HOGENOM; CLU_038813_0_1_12; -. DR OrthoDB; 356014at2; -. DR Proteomes; UP000000811; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR CDD; cd19962; PBP1_ABC_RfuA-like; 1. DR Gene3D; 3.40.50.2300; -; 2. DR InterPro; IPR028082; Peripla_BP_I. DR InterPro; IPR003760; PnrA-like. DR PANTHER; PTHR34296:SF2; ABC TRANSPORTER GUANOSINE-BINDING PROTEIN NUPN; 1. DR PANTHER; PTHR34296; TRANSCRIPTIONAL ACTIVATOR PROTEIN MED; 1. DR Pfam; PF02608; Bmp; 1. DR SUPFAM; SSF53822; Periplasmic binding protein-like I; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell inner membrane; Cell membrane; Lipoprotein; Membrane; KW Palmitate; Reference proteome; Signal; Transport. FT SIGNAL 1..19 FT /evidence="ECO:0000255" FT CHAIN 20..343 FT /note="ABC transporter riboflavin-binding protein RfuA" FT /id="PRO_0000018008" FT BINDING 43..46 FT /ligand="riboflavin" FT /ligand_id="ChEBI:CHEBI:57986" FT /evidence="ECO:0000269|PubMed:23404400, FT ECO:0007744|PDB:4IIL" FT BINDING 124 FT /ligand="riboflavin" FT /ligand_id="ChEBI:CHEBI:57986" FT /evidence="ECO:0000269|PubMed:23404400, FT ECO:0007744|PDB:4IIL" FT BINDING 140 FT /ligand="riboflavin" FT /ligand_id="ChEBI:CHEBI:57986" FT /evidence="ECO:0000269|PubMed:23404400, FT ECO:0007744|PDB:4IIL" FT BINDING 176 FT /ligand="riboflavin" FT /ligand_id="ChEBI:CHEBI:57986" FT /evidence="ECO:0000269|PubMed:23404400, FT ECO:0007744|PDB:4IIL" FT BINDING 208 FT /ligand="riboflavin" FT /ligand_id="ChEBI:CHEBI:57986" FT /evidence="ECO:0000269|PubMed:23404400, FT ECO:0007744|PDB:4IIL" FT BINDING 255 FT /ligand="riboflavin" FT /ligand_id="ChEBI:CHEBI:57986" FT /evidence="ECO:0000269|PubMed:23404400, FT ECO:0007744|PDB:4IIL" FT LIPID 20 FT /note="N-palmitoyl cysteine" FT /evidence="ECO:0000305|PubMed:23404400" FT LIPID 20 FT /note="S-diacylglycerol cysteine" FT /evidence="ECO:0000305|PubMed:23404400" FT STRAND 30..38 FT /evidence="ECO:0007829|PDB:4IIL" FT HELIX 44..61 FT /evidence="ECO:0007829|PDB:4IIL" FT TURN 62..64 FT /evidence="ECO:0007829|PDB:4IIL" FT STRAND 67..73 FT /evidence="ECO:0007829|PDB:4IIL" FT HELIX 78..80 FT /evidence="ECO:0007829|PDB:4IIL" FT HELIX 81..90 FT /evidence="ECO:0007829|PDB:4IIL" FT STRAND 95..101 FT /evidence="ECO:0007829|PDB:4IIL" FT HELIX 104..114 FT /evidence="ECO:0007829|PDB:4IIL" FT STRAND 120..124 FT /evidence="ECO:0007829|PDB:4IIL" FT STRAND 131..138 FT /evidence="ECO:0007829|PDB:4IIL" FT HELIX 140..156 FT /evidence="ECO:0007829|PDB:4IIL" FT STRAND 167..174 FT /evidence="ECO:0007829|PDB:4IIL" FT HELIX 177..181 FT /evidence="ECO:0007829|PDB:4IIL" FT HELIX 183..194 FT /evidence="ECO:0007829|PDB:4IIL" FT STRAND 199..204 FT /evidence="ECO:0007829|PDB:4IIL" FT STRAND 206..209 FT /evidence="ECO:0007829|PDB:4IIL" FT HELIX 211..224 FT /evidence="ECO:0007829|PDB:4IIL" FT STRAND 228..232 FT /evidence="ECO:0007829|PDB:4IIL" FT HELIX 234..236 FT /evidence="ECO:0007829|PDB:4IIL" FT HELIX 237..247 FT /evidence="ECO:0007829|PDB:4IIL" FT STRAND 250..256 FT /evidence="ECO:0007829|PDB:4IIL" FT HELIX 259..261 FT /evidence="ECO:0007829|PDB:4IIL" FT TURN 263..265 FT /evidence="ECO:0007829|PDB:4IIL" FT STRAND 266..272 FT /evidence="ECO:0007829|PDB:4IIL" FT HELIX 274..286 FT /evidence="ECO:0007829|PDB:4IIL" FT STRAND 294..298 FT /evidence="ECO:0007829|PDB:4IIL" FT HELIX 300..302 FT /evidence="ECO:0007829|PDB:4IIL" FT STRAND 304..307 FT /evidence="ECO:0007829|PDB:4IIL" FT HELIX 312..317 FT /evidence="ECO:0007829|PDB:4IIL" FT HELIX 320..335 FT /evidence="ECO:0007829|PDB:4IIL" FT STRAND 336..338 FT /evidence="ECO:0007829|PDB:4IIL" SQ SEQUENCE 343 AA; 37882 MW; 800687C5A1420C4D CRC64; MNGAVCVLSA LIAVFTCFSC RPAVQDERAV RIAVFVPGFR HDSPVYAMLC DGVERAVTQE RATGRSIGLD IIEAGPNQAL WREKLAHLAA EQRYRLIVSS NPALPHVLEP ILRQFPLQRF LVLDAYAPQE HSLITFRYNQ WEQAYLAGHL SALVSASAMR FANADKKIGL IAGQSYPVMT QTIIPAFLAG ARAVDPAFEV DVRVVGNWYD AAKSADLARI LFHEGVDVMM PICGGANQGV LAAARELGFY VSWFDDNGYA RAPGYVVGSS VMEQERLAYE QTLRCIRGEL PSAGAWTLGV KDGYVRFIEE DPLYLQTVPE PIRVRQSALL RRIQSGELTL PVR //